CN103555729B - 一种改造的trail基因序列、表达方法及应用 - Google Patents
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Classifications
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- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
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- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/177—Receptors; Cell surface antigens; Cell surface determinants
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70575—NGF/TNF-superfamily, e.g. CD70, CD95L, CD153, CD154
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
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- Chemical & Material Sciences (AREA)
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- Engineering & Computer Science (AREA)
- Biophysics (AREA)
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- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
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- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
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- Epidemiology (AREA)
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- Crystallography & Structural Chemistry (AREA)
- Analytical Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Priority Applications (10)
Application Number | Priority Date | Filing Date | Title |
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CN201310479275.3A CN103555729B (zh) | 2013-10-14 | 2013-10-14 | 一种改造的trail基因序列、表达方法及应用 |
DK14877744.4T DK2952523T3 (da) | 2013-10-14 | 2014-10-10 | Trail-mutant, der er membran-penetrerende og peptid-lignende, fremgangsmåde til fremstilling af samme og anvendelse deraf |
CN201480001787.1A CN105555799B (zh) | 2013-10-14 | 2014-10-10 | 一种trail穿膜肽样突变体、制备方法及应用 |
KR1020167008342A KR101871219B1 (ko) | 2013-10-14 | 2014-10-10 | Trail 막투과 펩타이드 유사 돌연변이체, 제조방법 및 응용 |
AU2014377142A AU2014377142B2 (en) | 2013-10-14 | 2014-10-10 | Trail membrane-penetrating peptide-like mutant, method of preparing same, and use thereof |
PCT/CN2014/088299 WO2015103894A1 (zh) | 2013-10-14 | 2014-10-10 | 一种trail穿膜肽样突变体、制备方法及应用 |
CA2925700A CA2925700C (en) | 2013-10-14 | 2014-10-10 | Trail membrane-penetrating peptide-like mutant, method of preparing same, and use thereof |
EP14877744.4A EP2952523B1 (en) | 2013-10-14 | 2014-10-10 | Trail membrane-penetrating peptide-like mutant, method of preparing same, and use thereof |
US14/764,740 US9499604B2 (en) | 2013-10-14 | 2014-10-10 | Trail mutant membrane-penetrating peptide-alike and methods of preparation thereof |
JP2016523912A JP6300913B2 (ja) | 2013-10-14 | 2014-10-10 | Trail細胞膜透過性ペプチド様突然変異体 |
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CN201310479275.3A CN103555729B (zh) | 2013-10-14 | 2013-10-14 | 一种改造的trail基因序列、表达方法及应用 |
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CN103555729A CN103555729A (zh) | 2014-02-05 |
CN103555729B true CN103555729B (zh) | 2016-08-24 |
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CN201310479275.3A Expired - Fee Related CN103555729B (zh) | 2013-10-14 | 2013-10-14 | 一种改造的trail基因序列、表达方法及应用 |
CN201480001787.1A Active CN105555799B (zh) | 2013-10-14 | 2014-10-10 | 一种trail穿膜肽样突变体、制备方法及应用 |
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CN201480001787.1A Active CN105555799B (zh) | 2013-10-14 | 2014-10-10 | 一种trail穿膜肽样突变体、制备方法及应用 |
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US (1) | US9499604B2 (da) |
EP (1) | EP2952523B1 (da) |
JP (1) | JP6300913B2 (da) |
KR (1) | KR101871219B1 (da) |
CN (2) | CN103555729B (da) |
AU (1) | AU2014377142B2 (da) |
CA (1) | CA2925700C (da) |
DK (1) | DK2952523T3 (da) |
WO (1) | WO2015103894A1 (da) |
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CN103555729B (zh) * | 2013-10-14 | 2016-08-24 | 成都华创生物技术有限公司 | 一种改造的trail基因序列、表达方法及应用 |
EP3266797B1 (en) * | 2015-03-02 | 2018-12-05 | Chengdu Huachuang Biotechnology Co., Ltd | Trail membrane-penetrating peptide-like mutant mur6, preparation method therefor, and application thereof |
WO2016138618A1 (zh) * | 2015-03-02 | 2016-09-09 | 成都华创生物技术有限公司 | TRAIL穿膜肽样突变体MuR5、制备方法及应用 |
CN108026181B (zh) * | 2015-10-22 | 2021-07-02 | 成都华创生物技术有限公司 | 一种TRAIL双靶点突变蛋白MuR6S4TR、其制备方法及其应用 |
CN110551205B (zh) * | 2018-06-01 | 2023-07-28 | 云南大学 | 可溶性人肿瘤坏死因子凋亡相关诱导配体的突变体及其制备方法和应用 |
CN109125709B (zh) * | 2018-08-23 | 2021-10-22 | 成都华创生物技术有限公司 | Trail突变体在制备治疗痤疮药物中的应用及一种制剂 |
CN115068590A (zh) * | 2021-03-10 | 2022-09-20 | 四川大学华西医院 | 一种肿瘤坏死因子相关凋亡诱导配体突变体的新用途 |
Family Cites Families (11)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE69635480T2 (de) * | 1995-06-29 | 2006-08-17 | Immunex Corp., Thousand Oaks | Apoptosis induzierendes cytokin |
CN1500808A (zh) * | 2002-11-15 | 2004-06-02 | 宏 李 | 重组人可溶性trail蛋白、其制备方法及其应用 |
CN1958794B (zh) * | 2005-11-03 | 2010-05-05 | 成都地奥九泓制药厂 | 人肿瘤坏死因子相关凋亡诱导配体突变体编码cDNA及制备方法和应用 |
GB0723059D0 (en) * | 2007-11-23 | 2008-01-02 | Nat Univ Ireland | Improved cytokine design |
GB0724532D0 (en) * | 2007-12-17 | 2008-01-30 | Nat Univ Ireland | Trail variants for treating cancer |
WO2010072228A1 (en) * | 2008-12-22 | 2010-07-01 | Xigen S.A. | Novel transporter constructs and transporter cargo conjugate molecules |
RU2548807C2 (ru) * | 2009-05-20 | 2015-04-20 | Торэй Индастриз, Инк. | Пептиды, проникающие в клетку |
US8461311B2 (en) * | 2010-06-08 | 2013-06-11 | Washington University | TRAIL trimers, methods and uses therefor |
CN102021173B (zh) * | 2010-07-30 | 2012-11-07 | 湖北大学 | 可溶性截短的人trail活性蛋白的制备方法 |
PL394618A1 (pl) * | 2011-04-19 | 2012-10-22 | Adamed Spólka Z Ograniczona Odpowiedzialnoscia | Przeciwnowotworowe bialko fuzyjne |
CN103555729B (zh) * | 2013-10-14 | 2016-08-24 | 成都华创生物技术有限公司 | 一种改造的trail基因序列、表达方法及应用 |
-
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Non-Patent Citations (5)
Title |
---|
Human Soluble TRAIL Protein Inducing Apoptosis in Osteosarcoma Cell;ZHU Shaobo等;《WUJNS》;20071231;第12卷(第6期);第1148-115页 * |
TRAIL and apoptosis induction by TNF-family death receptors;Wang shulin等;《Oncogene》;20031231;第22卷;第8628-8633页 * |
Venter等.EAW78466.1.《NCBI:GenBank》.2010, * |
李红梅等.人胎盘TRAIL基因cDNA的克隆和鉴定.《第四军医大学学报》.2008,第29卷(第3期),全文. * |
李红玲等.TNF相关的凋亡诱导配体与肿瘤.《国际病理科学与临床杂志》.2007,第27卷(第5期),第406-410页. * |
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KR20160048936A (ko) | 2016-05-04 |
US9499604B2 (en) | 2016-11-22 |
CA2925700C (en) | 2019-07-16 |
CN103555729A (zh) | 2014-02-05 |
EP2952523A4 (en) | 2016-06-01 |
CA2925700A1 (en) | 2015-07-16 |
WO2015103894A1 (zh) | 2015-07-16 |
JP6300913B2 (ja) | 2018-03-28 |
KR101871219B1 (ko) | 2018-06-27 |
CN105555799A (zh) | 2016-05-04 |
EP2952523A1 (en) | 2015-12-09 |
AU2014377142B2 (en) | 2017-07-20 |
DK2952523T3 (da) | 2017-11-06 |
AU2014377142A1 (en) | 2016-04-21 |
CN105555799B (zh) | 2020-04-17 |
JP2016538834A (ja) | 2016-12-15 |
US20160145317A1 (en) | 2016-05-26 |
EP2952523B1 (en) | 2017-08-09 |
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